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  • Bai, Y., Milne, J.S., Mayne, L., and Englander, S.W. 1993. Primary structure effects on peptide group hydrogen exchange. Proteins 17: 7586.
  • Barde, Y.A. 1990. The nerve growth factor family. Prog. Growth Factor Res. 2: 237248.
  • Bothwell, M.A. and Shooter, E.M. 1977. Dissociation equilibrium constant of β nerve growth factor. J. Biol. Chem. 252: 85328536.
  • Böttinger, E.P., Factor, V.M., Tsang, M.L., Weatherbee, J.A., Kopp, J.B., Qian, S.W., Wakefield, L.M., Roberts, A.B., Thorgeirsson, S.S., and Sporn, M.B. 1996. The recombinant proregion of transforming growth factor β1 (latency-associated peptide) inhibits active transforming growth factor β1 in transgenic mice. Proc. Natl. Acad. Sci. 93: 58775882.
  • Bradshaw, R.A., Blundell, T.L., Lapatto, R., McDonald, N.Q., and Murray-Rust, J. 1993. Nerve growth factor revisited. Trends Biochem. Sci. 18: 4852.
  • Buczek, O., Olivera, B.M., and Bulaj, G. 2004. Propeptide does not act as an intramolecular chaperone but facilitates protein disulfide isomerase-assisted folding of a conotoxin precursor. Biochemistry 43: 10931101.
  • Buevich, A.V., Shinde, U.P., Inouye, M., and Baum, J. 2001. Backbone dynamics of the natively unfolded pro-peptide of subtilisin by heteronuclear NMR relaxation studies. J. Biomol. NMR 20: 233249.
  • Casaccia-Bonnefil, P., Carter, B.D., Dobrowsky, R.T., and Chao, M.V. 1996. Death of oligodendrocytes mediated by the interaction of nerve growth factor with its receptor p75. Nature 383: 716719.
  • Cohen, P., Sutter, A., Landreth, G., Zimmermann, A., and Shooter, E.M. 1980. Oxidation of tryptophan-21 alters the biological activity and receptor binding characteristics of mouse nerve growth factor. J. Biol. Chem. 255: 29492954.
  • De Young, L.R., Burton, L.E., Liu, J., Powell, M.F., Schmelzer, C.H., and Skelton, N.J. 1996. RhNGF slow unfolding is not due to proline isomerization: Possibility of a cystine knot loop-threading mechanism. Protein Sci. 5: 15541566.
  • Degnin, C., Jean, F., Thomas, G., and Christian, J.L. 2004. Cleavages within the prodomain direct intracellular trafficking and degradation of mature bone morphogenetic protein-4. Mol. Biol. Cell 15: 50125020.
  • Drinkwater, C.C., Suter, U., Angst, C., and Shooter, E.M. 1991. Mutation of tryptophan-21 in mouse nerve growth factor (NGF) affects binding to the fast NGF receptor but not induction of neurites on PC12 cells. Proc. Biol. Sci. 246: 307313.
  • Eisenberg, D., Weiss, R.M., and Terwilliger, T.C. 1984. The hydrophobic moment detects periodicity in protein hydrophobicity. Proc. Natl. Acad. Sci. 81: 140144.
  • Ernfors, P., Ibanez, C.F., Ebendal, T., Olson, L., and Persson, H. 1990. Molecular cloning and neurotrophic activities of a protein with structural similarities to nerve growth factor: Developmental and topographical expression in the brain. Proc. Natl. Acad. Sci. 87: 54545458.
  • Fahnestock, M., Yu, G., and Coughlin, M.D. 2004. ProNGF: A neurotrophic or an apoptotic molecule? Prog. Brain Res. 146: 107110.
  • Fairlie, W.D., Zhang, H.P., Wu, W.M., Pankhurst, S.L., Bauskin, A.R., Russell, P.K., Brown, P.K., and Breit, S.N. 2001. The propeptide of the transforming growth factor-β superfamily member, macrophage inhibitory cytokine-1 (MIC-1), is a multifunctional domain that can facilitate protein folding and secretion. J. Biol. Chem. 276: 1691116918.
  • Feeney, B. and Clark, A.C. 2005. Reassembly of active caspase-3 is facilitated by the propeptide. J. Biol. Chem. 280: 3977239785.
  • Frade, J.M., Rodriguez-Tebar, A., and Barde, Y.A. 1996. Induction of cell death by endogenous nerve growth factor through its p75 receptor. Nature 383: 166168.
  • Gallagher, T., Gilliland, G., Wang, L., and Bryan, P. 1995. The prosegment-subtilisin BPN′ complex: Crystal structure of a specific ‘foldase.’. Structure 3: 907914.
  • Gray, A.M. and Mason, A.J. 1990. Requirement for activin A and transforming growth factor–β 1 pro-regions in homodimer assembly. Science 247: 13281330.
  • Hasan, W., Pedchenko, T., Krizsan-Agbas, D., Baum, L., and Smith, P.G. 2003. Sympathetic neurons synthesize and secrete pro-nerve growth factor protein. J. Neurobiol. 57: 3853.
  • He, X.L. and Garcia, K.C. 2004. Structure of nerve growth factor complexed with the shared neurotrophin receptor p75. Science 304: 870875.
  • Hidaka, Y., Ohno, M., Hemmasi, B., Hill, O., Forssmann, W.G., and Shimonishi, Y. 1998. In vitro disulfide-coupled folding of guanylyl cyclase-activating peptide and its precursor protein. Biochemistry 37: 84988507.
  • Hillger, F., Herr, G., Rudolph, R., and Schwarz, E. 2005. Biophysical comparison of BMP-2, ProBMP-2, and the free pro-peptide reveals stabilization of the pro-peptide by the mature growth factor. J. Biol. Chem. 280: 1497414980.
  • Hohn, A., Leibrock, J., Bailey, K., and Barde, Y.A. 1990. Identification and characterization of a novel member of the nerve growth factor/brain-derived neurotrophic factor family. Nature 344: 339341.
  • Ikemura, H., Takagi, H., and Inouye, M. 1987. Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli. J. Biol. Chem. 262: 78597864.
  • Jain, S.C., Shinde, U., Li, Y., Inouye, M., and Berman, H.M. 1998. The crystal structure of an autoprocessed Ser221Cys-subtilisin E-propeptide complex at 2.0 Å resolution. J. Mol. Biol. 284: 137144.
  • Kliemannel, M., Rattenholl, A., Golbik, R., Balbach, J., Lilie, H., Rudolph, R., and Schwarz, E. 2004. The mature part of proNGF induces the structure of its pro-peptide. FEBS Lett. 566: 207212.
  • LaLonde, J.M., Zhao, B., Janson, C.A., D'Alessio, K.J., McQueney, M.S., Orsini, M.J., Debouck, C.M., and Smith, W.W. 1999. The crystal structure of human procathepsin K. Biochemistry 38: 862869.
  • Lee, R., Kermani, P., Teng, K.K., and Hempstead, B.L. 2001. Regulation of cell survival by secreted proneurotrophins. Science 294: 19451948.
  • Lilie, H., Jaenicke, R., and Buchner, J. 1995. Characterization of a quaternary-structured folding intermediate of an antibody Fab-fragment. Protein Sci. 4: 917924.
  • McDonald, N.Q., Lapatto, R., Murray-Rust, J., Gunning, J., Wlodawer, A., and Blundell, T.L. 1991. New protein fold revealed by a 2.3-Å resolution crystal structure of nerve growth factor. Nature 354: 411414.
  • Nykjaer, A., Lee, R., Teng, K.K., Jansen, P., Madsen, P., Nielsen, M.S., Jacobsen, C., Kliemannel, M., Schwarz, E., and Willnow, T.E., et al. 2004. Sortilin is essential for proNGF-induced neuronal cell death. Nature 427: 843848.
  • Podobnik, M., Kuhelj, R., Turk, V., and Turk, D. 1997. Crystal structure of the wild-type human procathepsin B at 2.5 Å resolution reveals the native active site of a papain-like cysteine protease zymogen. J. Mol. Biol. 271: 774788.
  • Rattenholl, A., Lilie, H., Grossmann, A., Stern, A., Schwarz, E., and Rudolph, R. 2001a. The pro-sequence facilitates folding of human nerve growth factor from Escherichia coli inclusion bodies. Eur. J. Biochem. 268: 32963303.
  • Rattenholl, A., Ruoppolo, M., Flagiello, A., Monti, M., Vinci, F., Marino, G., Lilie, H., Schwarz, E., and Rudolph, R. 2001b. Pro-sequence assisted folding and disulfide bond formation of human nerve growth factor. J. Mol. Biol. 305: 523533.
  • Ruvinov, S., Wang, L., Ruan, B., Almog, O., Gilliland, G.L., Eisenstein, E., and Bryan, P.N. 1997. Engineering the independent folding of the subtilisin BPN′ prodomain: Analysis of two-state folding versus protein stability. Biochemistry 36: 1041410421.
  • Schmid, F.X. 1997. Spectral methods of characterizing protein conformation and conformational changes. In Protein structure: A practical approach (ed. T.E.Creighton), pp. 261297. IRL-Press, Oxford, United Kingdom.
  • Seidah, N.G., Benjannet, S., Pareek, S., Savaria, D., Hamelin, J., Goulet, B., Laliberte, J., Lazure, C., Chretien, M., and Murphy, R.A. 1996. Cellular processing of the nerve growth factor precursor by the mammalian pro-protein convertases. Biochem. J. 314: 951960.
  • Shinde, U. and Inouye, M. 2000. Intramolecular chaperones: Polypeptide extensions that modulate protein folding. Semin. Cell Dev. Biol. 11: 3544.
  • Shinde, U., Li, Y., Chatterjee, S., and Inouye, M. 1993. Folding pathway mediated by an intramolecular chaperone. Proc. Natl. Acad. Sci. 90: 69246928.
  • Sorenson, P., Winther, J.R., Kaarsholm, N.C., and Poulsen, F.M. 1993. The pro region required for folding of carboxypeptidase Y is a partially folded domain with little regular structural core. Biochemistry 32: 1216012166.
  • Timm, D.E. and Neet, K.E. 1992. Equilibrium denaturation studies of mouse β-nerve growth factor. Protein Sci. 1: 236244.
  • Weissman, J.S. and Kim, P.S. 1992. The pro region of BPTI facilitates folding. Cell 71: 841851.
  • Wiesmann, C., Ultsch, M.H., Bass, S.H., and de Vos, A.M. 1999. Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor. Nature 401: 184188.
  • Winther, J.R. and Sorensen, P. 1991. Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity. Proc. Natl. Acad. Sci. 88: 93309334.
  • Wise, R.J., Pittman, D.D., Handin, R.I., Kaufman, R.J., and Orkin, S.H. 1988. The propeptide of von Willebrand factor independently mediates the assembly of von Willebrand multimers. Cell 52: 229236.
  • Zhang, Z. and Smith, D.L. 1993. Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation. Protein Sci. 2: 522531.